3sqf

X-ray diffraction
1.63Å resolution

Crystal structure of monomeric M-PMV retroviral protease

Released:

Function and Biology Details

Reaction catalysed:
dUTP + H(2)O = dUMP + diphosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 13 kDa Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 12.9 KDa
Source organism: Mason-Pfizer monkey virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07570 (Residues: 760-873; Coverage: 13%)
Gene name: gag-pro
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 26.76Å b: 86.62Å c: 39.31Å
α: 90° β: 104.6° γ: 90°
R-values:
R R work R free
0.172 0.169 0.212
Expression system: Escherichia coli BL21(DE3)